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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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0.0026
NAD+
pH 7.2, 30°C
0.0045
NAD+
-
pH 7.3, 25°C
0.016
NAD+
-
25°C, pH 7.25, E175A mutant enzyme
0.017
NAD+
mutant enzyme M53A, at pH 7.3 and 25°C
0.0194
NAD+
-
pH 7.3, 25°C
0.02
NAD+
-
25°C, pH 7.25, E175A/A176R mutant enzyme
0.022
NAD+
mutant 17X-PTDH, pH 7.3, 25°C
0.022
NAD+
mutant enzyme E175A, at pH 7.3 and 25°C
0.032
NAD+
-
mutant M26I/E332N/C336D, pH 7.3, 25°C
0.034
NAD+
-
mutant D13E/M26I/E332N/C336D, pH 7.3, 25°C
0.036
NAD+
mutant Y139F, pH 7.3, 25°C
0.037
NAD+
-
mutant K330*, pH 7.3, 25°C
0.039
NAD+
-
mutant D13E/M26I/E175A/T181S/E332N/C336D, pH 7.3, 25°C
0.04
NAD+
-
mutant Q137R/I150F/Q215L/R275Q/L276Q/A319E/V315A/Q132R/V71I/E130K/I313L/A325V, pH 7.3, 25°C
0.04
NAD+
12 x PTDH mutant
0.0405
NAD+
-
pH 7.3, 25°C
0.041
NAD+
-
mutant D13E/M26I/E175A/E332N/C336D, pH 7.3, 25°C
0.045
NAD+
-
mutant D13E/M26I/E175A/T181S/A308T/E332N/C336D, pH 7.3, 25°C
0.046
NAD+
-
mutant Q132R/Q137R/I150F/Q215L/R275Q, pH 7.3, 25°C
0.05
NAD+
-
mutant Q137R/I150F/Q215L/R275Q/L276Q/A319E/V315A/A325V, pH 7.3, 25°C
0.052
NAD+
-
mutant Q137R/I150F/Q215L/R275Q/A319E, pH 7.3, 25°C
0.0522
NAD+
wild-type, pH 7.3, 25°C
0.053
NAD+
-
25°C, pH 7.25, wild type enzyme
0.053
NAD+
-
wild-type, pH 7.3, 25°C
0.056
NAD+
-
pH 7.2, 30°C
0.056
NAD+
-
mutant Q137R/I150F/Q215L/R275Q/L276Q, pH 7.3, 25°C
0.057
NAD+
-
pH 7.5, 25°C, wild type enzyme
0.057
NAD+
-
mutant Q137R/I150F/Q215L/R275Q/L276Q/A319E/V315A/Q132R, pH 7.3, 25°C
0.06
NAD+
-
25°C, pH 7.25, A176R mutant enzyme
0.06
NAD+
-
mutant Q132R, pH 7.3, 25°C
0.063
NAD+
-
mutant Q137R/I150F/Q215L/R275Q/L276Q/A319E/V315A/V71I, pH 7.3, 25°C
0.064
NAD+
-
mutant Q215L, pH 7.3, 25°C
0.064
NAD+
mutant enzyme M53N, at pH 7.3 and 25°C
0.065
NAD+
-
mutant Q137R/I150F/Q215L/R275Q/D162N/V315A, pH 7.3, 25°C
0.066
NAD+
-
mutant Q137R, pH 7.3, 25°C
0.066
NAD+
-
mutant Q137R/I150F/Q215L/R275Q/L276Q/A319E/V315A, pH 7.3, 25°C
0.066
NAD+
-
wild-type, pH 7.3, 25°C
0.07
NAD+
-
mutant R275Q, pH 7.3, 25°C
0.071
NAD+
-
mutant Q137R/I150F/Q215L/R275Q/L276Q/A319E/V315A/I313L, pH 7.3, 25°C
0.074
NAD+
-
mutant Q137R/I150F/Q215L/R275Q, pH 7.3, 25°C
0.074
NAD+
mutant R301K, pH 7.3, 25°C
0.075
NAD+
-
mutant I150F, pH 7.3, 25°C
0.075
NAD+
-
mutant Q137R/I150F/Q215L/R275Q/L276Q/A319E/V315A/E130K, pH 7.3, 25°C
0.102
NAD+
mutant W134F, pH 7.3, 25°C
0.11
NAD+
-
pH 7.5, 25°C, K76R mutant enzyme
0.128
NAD+
-
pH 7.2, 40°C
0.187
NAD+
mutant W134A, pH 7.3, 25°C
0.2
NAD+
-
pH 7.5, 25°C, K76C mutant enzyme
0.216
NAD+
mutant R301A, pH 7.3, 25°C
0.25
NAD+
mutant S295A, pH 7.3, 25°C
0.26
NAD+
-
pH 7.5, 25°C, K76A mutant enzyme
0.9
NAD+
-
pH 7.5, 25°C, K76M mutant enzyme
1
NAD+
-
pH 7.5, 25°C, E266Q mutant enzyme
1
NAD+
-
pH 7.5, 25°C, R237K mutant enzyme
0.004
NADP+
-
25°C, pH 7.25, E175A/A176R mutant enzyme
0.056
NADP+
-
mutant D13E/M26I/E175A/T181S/A308T/E332N/C336D, pH 7.3, 25°C
0.057
NADP+
-
mutant D13E/M26I/E175A/T181S/E332N/C336D, pH 7.3, 25°C
0.065
NADP+
-
mutant D13E/M26I/E175A/E332N/C336D, pH 7.3, 25°C
0.077
NADP+
-
25°C, pH 7.25, A176R mutant enzyme
0.14
NADP+
-
mutant E175A, pH 7.3, 25°C
0.144
NADP+
-
25°C, pH 7.25, E175A mutant enzyme
1.07
NADP+
-
mutant D13E/M26I/E332N/C336D, pH 7.3, 25°C
2.5
NADP+
-
wild-type, pH 7.3, 25°C
2.51
NADP+
-
25°C, pH 7.25, wild type enzyme
0.001
phosphite
-
mutant R237K
0.014
phosphite
-
cosubstrate NAD+, mutant K330*, pH 7.3, 25°C
0.027
phosphite
-
cosubstrate NAD+, mutant M26I/E332N/C336D, pH 7.3, 25°C
0.03
phosphite
-
cosubstrate NAD+, mutant D13E/M26I/E332N/C336D, pH 7.3, 25°C
0.035
phosphite
-
mutant D79N
0.045
phosphite
-
mutant Q132R, pH 7.3, 25°C
0.046
phosphite
-
mutant Q137R/I150F/Q215L/R275Q/L276Q/A319E/V315A/Q132R/V71I/E130K/I313L/A325V, pH 7.3, 25°C
0.046
phosphite
12 x PTDH mutant
0.047
phosphite
-
cosubstrate NAD+, wild-type, pH 7.3, 25°C
0.048
phosphite
-
cosubstrate NAD+, mutant D13E/M26I/E175A/T181S/A308T/E332N/C336D, pH 7.3, 25°C
0.048
phosphite
-
mutant Q137R, pH 7.3, 25°C
0.055
phosphite
-
wild-type
0.057
phosphite
-
wild-type, pH 7.3, 25°C
0.057
phosphite
parent enzyme
0.058
phosphite
-
mutant Q215L, pH 7.3, 25°C
0.062
phosphite
-
cosubstrate NADP+, mutant D13E/M26I/E175A/T181S/E332N/C336D, pH 7.3, 25°C
0.07
phosphite
-
cosubstrate NADP+, mutant D13E/M26I/E175A/T181S/A308T/E332N/C336D, pH 7.3, 25°C
0.075
phosphite
-
mutant Q132R/Q137R/I150F/Q215L/R275Q, pH 7.3, 25°C
0.078
phosphite
-
mutant R275Q, pH 7.3, 25°C
0.079
phosphite
Opt12 variant
0.082
phosphite
-
cosubstrate NAD+, mutant D13E/M26I/E175A/E332N/C336D, pH 7.3, 25°C
0.084
phosphite
-
cosubstrate NAD+, mutant D13E/M26I/E175A/T181S/E332N/C336D, pH 7.3, 25°C
0.087
phosphite
-
cosubstrate NADP+, mutant D13E/M26I/E175A/E332N/C336D, pH 7.3, 25°C
0.09
phosphite
Opt13 variant
0.092
phosphite
-
mutant Q137R/I150F/Q215L/R275Q/A319E, pH 7.3, 25°C
0.096
phosphite
-
mutant Q137R/I150F/Q215L/R275Q/L276Q/A319E/V315A, pH 7.3, 25°C
0.099
phosphite
-
mutant I150F, pH 7.3, 25°C
0.105
phosphite
-
mutant Q137R/I150F/Q215L/R275Q/L276Q/A319E/V315A/V71I, pH 7.3, 25°C
0.12
phosphite
-
mutant Q137R/I150F/Q215L/R275Q/L276Q, pH 7.3, 25°C
0.123
phosphite
-
mutant Q137R/I150F/Q215L/R275Q/L276Q/A319E/V315A/E130K, pH 7.3, 25°C
0.135
phosphite
-
mutant Q137R/I150F/Q215L/R275Q/L276Q/A319E/V315A/A325V, pH 7.3, 25°C
0.138
phosphite
-
cosubstrate NADP+, mutant E175A, pH 7.3, 25°C
0.142
phosphite
Opt14 variant
0.144
phosphite
-
mutant Q137R/I150F/Q215L/R275Q, pH 7.3, 25°C
0.155
phosphite
-
mutant Q137R/I150F/Q215L/R275Q/D162N/V315A, pH 7.3, 25°C
0.156
phosphite
-
mutant Q137R/I150F/Q215L/R275Q/L276Q/A319E/V315A/I313L, pH 7.3, 25°C
0.169
phosphite
-
mutant Q137R/I150F/Q215L/R275Q/L276Q/A319E/V315A/Q132R, pH 7.3, 25°C
0.475
phosphite
pH 7.0, 25°C
1.2
phosphite
-
mutant D79A
1.9
phosphite
-
cosubstrate NADP+, mutant D13E/M26I/E332N/C336D, pH 7.3, 25°C
1.9
phosphite
-
cosubstrate NADP+, wild-type, pH 7.3, 25°C
0.0073
phosphonate
-
pH 7.2, 30°C
0.0087
phosphonate
pH 7.2, 30°C
0.017
phosphonate
mutant enzyme M53N, at pH 7.3 and 25°C
0.024
phosphonate
pH 7.2, 40°C
0.0254
phosphonate
-
pH 7.3, 25°C
0.028
phosphonate
mutant 17X-PTDH, pH 7.3, 25°C
0.028
phosphonate
wild type enzyme, at pH 7.3 and 25°C
0.028
phosphonate
mutant enzyme E175A, at pH 7.3 and 25°C
0.039
phosphonate
mutant Y139F, pH 7.3, 25°C
0.053
phosphonate
-
pH 7.5, 25°C, wild type enzyme
0.0549
phosphonate
-
pH 7.3, 25°C
0.0811
phosphonate
wild-type, pH 7.3, 25°C
0.1
phosphonate
mutant enzyme M53A, at pH 7.3 and 25°C
0.103
phosphonate
mutant S295A, pH 7.3, 25°C
0.201
phosphonate
-
at pH 7.5 and 30°C
0.237
phosphonate
-
pH 7.3, 25°C
0.238
phosphonate
mutant W134F, pH 7.3, 25°C
0.287
phosphonate
-
pH 7.2, 40°C
0.35
phosphonate
-
pH 7.5, 25°C, K76R mutant enzyme
0.6
phosphonate
-
pH 7.5, 25°C, K76C mutant enzyme
1.1
phosphonate
-
pH 7.5, 25°C, K76A mutant enzyme
1.1
phosphonate
mutant enzyme R301K, at pH 7.3 and 25°C
1.11
phosphonate
mutant R301K, pH 7.3, 25°C
1.91
phosphonate
mutant W134A, pH 7.3, 25°C
2
phosphonate
-
pH 7.5, 25°C, K76M mutant enzyme
5
phosphonate
-
pH 7.5, 25°C, E266Q mutant enzyme
6
phosphonate
-
pH 7.5, 25°C, R237K mutant enzyme
19.4
phosphonate
mutant R301A, pH 7.3, 25°C
20
phosphonate
mutant enzyme R301A, at pH 7.3 and 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2.8
NAD+
-
mutant K330*, pH 7.3, 25°C
2.8
NAD+
-
mutant Q132R/Q137R/I150F/Q215L/R275Q, pH 7.3, 25°C
2.85
NAD+
-
mutant Q137R/I150F/Q215L/R275Q/D162N/V315A, pH 7.3, 25°C
2.9
NAD+
-
mutant Q137R/I150F/Q215L/R275Q/L276Q, pH 7.3, 25°C
2.9
NAD+
-
mutant Q137R/I150F/Q215L/R275Q/L276Q/A319E/V315A, pH 7.3, 25°C
2.9
NAD+
-
wild-type, pH 7.3, 25°C
2.93
NAD+
-
25°C, pH 7.25, wild type enzyme
3.13
NAD+
-
mutant Q132R, pH 7.3, 25°C
3.2
NAD+
-
mutant Q137R/I150F/Q215L/R275Q/A319E, pH 7.3, 25°C
3.2
NAD+
-
mutant Q137R/I150F/Q215L/R275Q/L276Q/A319E/V315A/Q132R, pH 7.3, 25°C
3.2
NAD+
-
mutant Q137R/I150F/Q215L/R275Q/L276Q/A319E/V315A/Q132R/V71I/E130K/I313L/A325V, pH 7.3, 25°C
3.5
NAD+
-
25°C, pH 7.25, E175A mutant enzyme
3.5
NAD+
-
mutant Q137R/I150F/Q215L/R275Q/L276Q/A319E/V315A/A325V, pH 7.3, 25°C
3.5
NAD+
-
mutant Q137R/I150F/Q215L/R275Q/L276Q/A319E/V315A/E130K, pH 7.3, 25°C
3.5
NAD+
-
mutant Q137R/I150F/Q215L/R275Q/L276Q/A319E/V315A/I313L, pH 7.3, 25°C
3.5
NAD+
-
mutant Q137R/I150F/Q215L/R275Q/L276Q/A319E/V315A/V71I, pH 7.3, 25°C
3.6
NAD+
-
mutant M26I/E332N/C336D, pH 7.3, 25°C
3.6
NAD+
-
mutant Q137R/I150F/Q215L/R275Q, pH 7.3, 25°C
3.7
NAD+
-
mutant D13E/M26I/E332N/C336D, pH 7.3, 25°C
3.94
NAD+
-
25°C, pH 7.25, E175A/A176R mutant enzyme
3.96
NAD+
-
mutant Q132R, pH 7.3, 25°C
4
NAD+
-
mutant D13E/M26I/E175A/E332N/C336D, pH 7.3, 25°C
4.1
NAD+
-
mutant R275Q, pH 7.3, 25°C
4.28
NAD+
-
25°C, pH 7.25, A176R mutant enzyme
4.3
NAD+
-
mutant D13E/M26I/E175A/T181S/E332N/C336D, pH 7.3, 25°C
4.4
NAD+
-
mutant I150F, pH 7.3, 25°C
4.4
NAD+
-
wild-type, pH 7.3, 25°C
4.6
NAD+
-
mutant Q215L, pH 7.3, 25°C
4.75
NAD+
-
mutant Q137R, pH 7.3, 25°C
5.7
NAD+
-
mutant D13E/M26I/E175A/T181S/A308T/E332N/C336D, pH 7.3, 25°C
1.4
NADP+
-
wild-type, pH 7.3, 25°C
1.41
NADP+
-
25°C, pH 7.25, wild type enzyme
1.75
NADP+
-
mutant D13E/M26I/E332N/C336D, pH 7.3, 25°C
1.8
NADP+
-
mutant D13E/M26I/E175A/E332N/C336D, pH 7.3, 25°C
1.8
NADP+
-
mutant D13E/M26I/E175A/T181S/E332N/C336D, pH 7.3, 25°C
1.9
NADP+
-
25°C, pH 7.25, E175A/A176R mutant enzyme
1.9
NADP+
-
mutant D13E/M26I/E175A/T181S/A308T/E332N/C336D, pH 7.3, 25°C
2.18
NADP+
-
25°C, pH 7.25, A176R mutant enzyme
2.18
NADP+
-
25°C, pH 7.25, E175A mutant enzyme
2.2
NADP+
-
mutant E175A, pH 7.3, 25°C
0.0126
phosphite
-
mutant R237K
0.0305
phosphite
-
mutant D79A
0.23
phosphite
-
mutant D79N
0.58
phosphite
-
mutant NADP-12X NAD
0.621
phosphite
-
mutant K76A
2.04
phosphite
-
mutant NADP-12X NAD
2.42
phosphite
-
wild-type
3.25
phosphite
12 x PTDH mutant
3.26
phosphite
-
thermostable mutant 12X-PTDH
3.55
phosphite
Opt12 and Opt13 variants
3.65
phosphite
Opt14 variant
4.367
phosphite
parent enzyme
7.5
phosphite
-
mutant E266Q
0.016
phosphonate
mutant enzyme M53N, at pH 7.3 and 25°C
0.041
phosphonate
mutant R301A, pH 7.3, 25°C
0.059
phosphonate
mutant enzyme M53A, at pH 7.3 and 25°C
0.28
phosphonate
-
pH 7.5, 25°C, R237K mutant enzyme
0.58
phosphonate
-
pH 7.5, 25°C, K76C mutant enzyme
0.82
phosphonate
-
pH 7.5, 25°C, K76A mutant enzyme
1.62
phosphonate
-
pH 7.5, 25°C, K76M mutant enzyme
1.73
phosphonate
mutant W134A, pH 7.3, 25°C
1.87
phosphonate
-
at pH 7.5 and 30°C
2.33
phosphonate
-
pH 7.5, 25°C, K76R mutant enzyme
2.53
phosphonate
mutant S295A, pH 7.3, 25°C
2.96
phosphonate
mutant W134F, pH 7.3, 25°C
3.1
phosphonate
mutant enzyme E175A, at pH 7.3 and 25°C
3.2
phosphonate
-
pH 7.5, 25°C, wild type enzyme
3.27
phosphonate
mutant 17X-PTDH, pH 7.3, 25°C
3.36
phosphonate
-
pH 7.3, 25°C
3.68
phosphonate
mutant Y139F, pH 7.3, 25°C
4.5
phosphonate
mutant R301K, pH 7.3, 25°C
5.1
phosphonate
-
pH 7.3, 25°C
6.57
phosphonate
wild-type, pH 7.3, 25°C
6.83
phosphonate
-
pH 7.3, 25°C
8
phosphonate
-
pH 7.5, 25°C, E266Q mutant enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
R301A
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation R301A leads to sharp decrease in activity, while kcat value is similar to wild-type
R301K
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation R301K leads to sharp decrease in activity, while kcat value is similar to wild-type
S295A
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation S295A leads to sharp decrease in activity, while kcat value is similar to wild-type
W134A
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation W134A leads to sharp decrease in activity, while kcat value is similar to wild-type
W134F
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation W134F leads to sharp decrease in activity, while kcat value is similar to wild-type
Y139F
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation Y139F leads to sharp decrease in activity, while kcat value is similar to wild-type
R301A
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation R301A leads to sharp decrease in activity, while kcat value is similar to wild-type
-
R301K
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation R301K leads to sharp decrease in activity, while kcat value is similar to wild-type
-
W134A
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation W134A leads to sharp decrease in activity, while kcat value is similar to wild-type
-
Y139F
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation Y139F leads to sharp decrease in activity, while kcat value is similar to wild-type
-
R301A
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation R301A leads to sharp decrease in activity, while kcat value is similar to wild-type
R301K
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation R301K leads to sharp decrease in activity, while kcat value is similar to wild-type
S295A
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation S295A leads to sharp decrease in activity, while kcat value is similar to wild-type
W134A
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation W134A leads to sharp decrease in activity, while kcat value is similar to wild-type
W134F
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation W134F leads to sharp decrease in activity, while kcat value is similar to wild-type
Y139F
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation Y139F leads to sharp decrease in activity, while kcat value is similar to wild-type
R301A
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation R301A leads to sharp decrease in activity, while kcat value is similar to wild-type
-
R301K
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation R301K leads to sharp decrease in activity, while kcat value is similar to wild-type
-
W134A
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation W134A leads to sharp decrease in activity, while kcat value is similar to wild-type
-
Y139F
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation Y139F leads to sharp decrease in activity, while kcat value is similar to wild-type
-
R301A
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation R301A leads to sharp decrease in activity, while kcat value is similar to wild-type
R301K
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation R301K leads to sharp decrease in activity, while kcat value is similar to wild-type
S295A
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation S295A leads to sharp decrease in activity, while kcat value is similar to wild-type
W134A
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation W134A leads to sharp decrease in activity, while kcat value is similar to wild-type
W134F
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation W134F leads to sharp decrease in activity, while kcat value is similar to wild-type
Y139F
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation Y139F leads to sharp decrease in activity, while kcat value is similar to wild-type
A146S
increases the half-life of thermal inactivation at 45°C from around 1 min to 8 min
A176R
-
strongly decreased Km for NADP+
A319E
increases the half-life of thermal inactivation at 45°C from around 1 min to 2 min
A319E/T101A
increases the half-life of thermal inactivation at 45°C from around 1 min to 5 min
A325V
thermostability almost identical to that of the wild-type enzyme
C336D
increases solubility and activity, thermostability almost identical to that of the wild-type enzyme
D13E
increases solubility and activity, thermostability almost identical to that of the wild-type enzyme
D13E/M26I/E175A/E332N/C336D
-
mutant obtained by directed evolution, round 4
D13E/M26I/E175A/T181S/A308T/E332N/C336D
-
mutant obtained by directed evolution, round 6, strong decrease in KM value for NADP compared to wild-type
D13E/M26I/E175A/T181S/E332N/C336D
-
mutant obtained by directed evolution, round 5
D13E/M26I/E332N/C336D
-
mutant obtained by directed evolution, round 3
D13E/M26I/V71I/E130K/Q132R/Q137R/I150F/E175A/Q215L/R275Q/L276Q/I313L/V315A/A319E/A325V/E332N/C336D
thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity. Mutation E175A leads to relaxation of cofactor specificity
D79A
-
significant differences in its kinetic constants compared to the wild-type enzyme. 2600fold decrease in catalytic efficiency. Pre-steady-state rates are approximately the same as the steady-state rates
D79N
-
has kinetic parameters more similar to those of wild-type
E130K
increases the half-life of thermal inactivation at 45°C from around 1 min to 12.5 min
E130Q
increases the half-life of thermal inactivation at 45°C from around 1 min to 7 min
E130R
increases the half-life of thermal inactivation at 45°C from around 1 min to 9 min
E332N
increases solubility and activity, thermostability almost identical to that of the wild-type enzyme
F198I
leads to low activity
F198M
increases the half-life of thermal inactivation at 45°C from around 1 min to 2 min
H292Q
-
no activity, NAD+ binding is abolished
I313L
thermostability almost identical to that of the wild-type enzyme
K330*
-
mutant obtained by directed evolution, round 1
K76C
-
significant increase in Km for both substrates
K76M
-
significant increase in Km for both substrates
K76R
-
significant increase in Km for both substrates
L276C
increases the half-life of thermal inactivation at 45°C from around 1 min to 12 min
L276H
increases the half-life of thermal inactivation at 45°C from around 1 min to 2 min
L276Q
increases the half-life of thermal inactivation at 45°C from around 1 min to 3.5 min
L276R
increases the half-life of thermal inactivation at 45°C from around 1 min to 8 min
L276S
increases the half-life of thermal inactivation at 45°C from around 1 min to 3 min
M26I
increases solubility and activity, thermostability almost identical to that of the wild-type enzyme
M26I/E332N/C336D
-
mutant obtained by directed evolution, round 2
M53A
the KM values for phosphonate and NAD+ are little different from the parent enzyme, while kcat is reduced by a factor of 50
M53N
the KM values for phosphonate and NAD+ are little different from the parent enzyme, while kcat is reduced by a factor of 200
Q132K
increases the half-life of thermal inactivation at 45°C from around 1 min to 3 min
Q132R/Q137R/I150F/Q215L/R275Q
-
thermostable mutant, half-life at 45°C 161 min compared to 1.4 min of wild-type
Q137H
increases the half-life of thermal inactivation at 45°C from around 1 min to 4.5 min
Q137R/I150F/Q215L/R275Q
-
thermostable mutant, half-life at 45°C 200 min compared to 1.4 min of wild-type
Q137R/I150F/Q215L/R275Q/A319E
-
thermostable mutant, half-life at 45°C 567 min compared to 1.4 min of wild-type
Q137R/I150F/Q215L/R275Q/D162N/V315A
-
thermostable mutant, half-life at 45°C 614 min compared to 1.4 min of wild-type
Q137R/I150F/Q215L/R275Q/L276Q
-
thermostable mutant, half-life at 45°C 437 min compared to 1.4 min of wild-type
Q137R/I150F/Q215L/R275Q/L276Q/A319E/V315A
-
thermostable mutant, half-life at 45°C 1421 min compared to 1.4 min of wild-type
Q137R/I150F/Q215L/R275Q/L276Q/A319E/V315A/A325V
-
thermostable mutant, half-life at 45°C 2315 min compared to 1.4 min of wild-type
Q137R/I150F/Q215L/R275Q/L276Q/A319E/V315A/E130K
-
thermostable mutant, half-life at 45°C 1515 min compared to 1.4 min of wild-type
Q137R/I150F/Q215L/R275Q/L276Q/A319E/V315A/I313L
-
thermostable mutant, half-life at 45°C 1765 min compared to 1.4 min of wild-type
Q137R/I150F/Q215L/R275Q/L276Q/A319E/V315A/Q132R
-
thermostable mutant, half-life at 45°C 2350 min compared to 1.4 min of wild-type
Q137R/I150F/Q215L/R275Q/L276Q/A319E/V315A/Q132R/V71I/E130K/I313L/A325V
-
thermostable mutant, half-life at 45°C 8440 min compared to 1.4 min of wild-type
Q137R/I150F/Q215L/R275Q/L276Q/A319E/V315A/Q132R/V71I/E130K/I313L/A325V/A176R
-
highly stable and active mutant engineered for regeneration of NADPH and enzyme membrane reactors
Q137R/I150F/Q215L/R275Q/L276Q/A319E/V315A/V71I
-
thermostable mutant, half-life at 45°C 2000 min compared to 1.4 min of wild-type
Q215M
increases the half-life of thermal inactivation at 45°C from around 1 min to 2.5 min
R237H
-
almost complete loss of activity
R237L
-
almost complete loss of activity
R237Q
-
almost complete loss of activity
R275L
increases the half-life of thermal inactivation at 45°C from around 1 min to 9 min
S295A
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation S295A leads to sharp decrease in activity, while kcat value is similar to wild-type
T101A
increases the half-life of thermal inactivation at 45°C from around 1 min to 4.5 min
V315A
thermostability almost identical to that of the wild-type enzyme
V71Ia
thermostability almost identical to that of the wild-type enzyme
W134A
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation W134A leads to sharp decrease in activity, while kcat value is similar to wild-type
W134F
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation W134F leads to sharp decrease in activity, while kcat value is similar to wild-type
Y139F
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation Y139F leads to sharp decrease in activity, while kcat value is similar to wild-type
E266Q
-
significant increase in Km for both substrates, increase in turnover
-
H292N
-
almost complete loss of activity
-
K76A
-
significant increase in Km for both substrates
-
K76M
-
significant increase in Km for both substrates
-
K76R
-
significant increase in Km for both substrates
-
E175A
-
the mutation allows the enzyme to use both NAD+ and NADP+
-
E175A/A176R
-
double mutant, 3.6-fold higher efficiency with NAD+, 1000-fold higher efficiency with NADP+, 3-fold favor for NADP+ over NAD+ as cofactor
-
H292F
-
no activity, NAD+ binding is abolished
-
H292K
-
no activity, NAD+ binding is abolished
-
H292N
-
no activity, NAD+ binding is abolished
-
M53A
-
the KM values for phosphonate and NAD+ are little different from the parent enzyme, while kcat is reduced by a factor of 50
-
M53N
-
the KM values for phosphonate and NAD+ are little different from the parent enzyme, while kcat is reduced by a factor of 200
-
R237K
-
strong increase in Km for both substrates, reduced Vmax
-
R301A
-
the mutant shows about 100fold loss in kcat and a 500fold increased Km value for phosphonate. The Ki value of sulfite with the mutant is 400fold increased compared to the wild type enzyme
-
R301K
-
the mutant exhibits a slightly higher kcat than the wild type enzyme and a 20fold increased Km value for phosphonate
-
D79A
-
significant differences in its kinetic constants compared to the wild-type enzyme. 2600fold decrease in catalytic efficiency. Pre-steady-state rates are approximately the same as the steady-state rates
-
E266Q
-
higher activity, steady-state and pre-steady-state rates are comparable
-
K76A
-
pre-steady-state rates are approximately the same as the steady-state rates
-
R237K
-
low activity, absence of a significant burst in the pre-steady-state
-
E175A
-
strongly decreased Km for NADP+
E175A
-
mutant with significantly increased kcat value for NADP+
E175A
increases solubility and activity, thermostability almost identical to that of the wild-type enzyme
E175A
the mutation allows the enzyme to use both NAD+ and NADP+
E175A/A176R
-
double mutant, 3.6-fold higher efficiency with NAD+, 1000-fold higher efficiency with NADP+, 3-fold favor for NADP+ over NAD+ as cofactor
E175A/A176R
-
mutant utilizes both NAD+ and NADP+, kinetic isotope effects study, hydride transfer step is partially rate determining
E266Q
-
significant increase in Km for both substrates, increase in turnover
E266Q
-
higher activity, steady-state and pre-steady-state rates are comparable
H292F
-
almost complete loss of activity
H292F
-
no activity, NAD+ binding is abolished
H292K
-
almost complete loss of activity
H292K
-
no activity, NAD+ binding is abolished
H292N
-
almost complete loss of activity
H292N
-
no activity, NAD+ binding is abolished
I150F
-
thermostable mutant, half-life at 45°C 7.0 min compared to 1.4 min of wild-type
I150F
increases the half-life of thermal inactivation at 45°C from around 1 min to 7 min
K76A
-
significant increase in Km for both substrates
K76A
-
pre-steady-state rates are approximately the same as the steady-state rates
Q132R
-
thermostable mutant, half-life at 45°C 2.3 min compared to 1.4 min of wild-type
Q132R
increases the half-life of thermal inactivation at 45°C from around 1 min to 2 min
Q137R
-
thermostable mutant, half-life at 45°C 3.8 min compared to 1.4 min of wild-type
Q137R
increases the half-life of thermal inactivation at 45°C from around 1 min to 4 min
Q215L
-
thermostable mutant, half-life at 45°C 8.7 min compared to 1.4 min of wild-type
Q215L
increases the half-life of thermal inactivation at 45°C from around 1 min to 9 min
R237K
-
significant increase in Km for both substrates
R237K
-
strong increase in Km for both substrates, reduced Vmax
R237K
-
low activity, absence of a significant burst in the pre-steady-state
R275Q
-
thermostable mutant, half-life at 45°C 4.6 min compared to 1.4 min of wild-type
R275Q
increases the half-life of thermal inactivation at 45°C from around 1 min to 4.5 min
R301A
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation R301A leads to sharp decrease in activity, while kcat value is similar to wild-type
R301A
the mutant shows about 100fold loss in kcat and a 500fold increased Km value for phosphonate. The Ki value of sulfite with the mutant is 400fold increased compared to the wild type enzyme
R301K
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation R301K leads to sharp decrease in activity, while kcat value is similar to wild-type
R301K
the mutant exhibits a slightly higher kcat than the wild type enzyme and a 20fold increased Km value for phosphonate
additional information
-
mutant 17x-PTDH is based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+
additional information
-
mutant 17x-PTDH is based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+
-
additional information
-
mutant 17x-PTDH is based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+
additional information
-
mutant 17x-PTDH is based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+
-
additional information
-
mutant 17x-PTDH is based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+
additional information
12 x PTDH mutant, saturation mutagenesis performed separately on each of the following residues in the parent PTDH template: V71, E130, Q132, Q137, I150, Q215, R275, L276, I313, V315, A319, and A325. The most thermostabilizing mutation discovered for each particular site is incorporated into the 12 x PTDH mutant, performed for K132, H137, L275, and C276, forming an optimized thermally stable phosphite dehydrogenase termed Opt12. Addition of A146S to Opt12 leads to the Opt13 variant, and the further addition of F198M leads to Opt14
additional information
-
thermostable mutant 12X-PTDH with higher solubility than the wild-type. Thermostable mutant with dual cofactor specificity NADP-12X NAD shows pre-steady-state behavior very similar to that observed with 12X-PTDH and the wild-type enzyme. Pre-steady-state traces of thermostable mutant with dual cofactor specificity NADP-12X NADP shows curvature with NADP, particularly with protiated phosphite
additional information
mutant 17x-PTDH is based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+
additional information
-
mutant 17x-PTDH is based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+
additional information
-
thermostable mutant 12X-PTDH with higher solubility than the wild-type. Thermostable mutant with dual cofactor specificity NADP-12X NAD shows pre-steady-state behavior very similar to that observed with 12X-PTDH and the wild-type enzyme. Pre-steady-state traces of thermostable mutant with dual cofactor specificity NADP-12X NADP shows curvature with NADP, particularly with protiated phosphite
-
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Costas, A.M.G.; White, A.K.; Metcalf, W.W.
Purification and characterization of a novel phosphorus-oxidizing enzyme from Pseudomonas stutzeri WM88
J. Biol. Chem.
276
17429-17436
2001
Pseudomonas stutzeri (O69054)
brenda
Vrtis, J.M.; White, A.K.; Metcalf, W.W.; van der Donk, W.A.
Phosphite dehydrogenase: An unusual phosphoryl transfer reaction
J. Am. Chem. Soc.
123
2672-2673
2001
Pseudomonas stutzeri
brenda
Woodyer, R.; van der Donk, W.A.; Zhao, H.
Relaxing the nicotinamide cofactor specificity of phosphite dehydrogenase by rational design
Biochemistry
42
11604-11614
2003
Pseudomonas stutzeri
brenda
Woodyer, R.; Wheatley, J.L.; Relyea, H.A.; Rimkus, S.; van der Donk, W.A.
Site-directed mutagenesis of active site residues of phosphite dehydrogenase
Biochemistry
44
4765-4774
2005
Pseudomonas stutzeri, Pseudomonas stutzeri WM 88
brenda
Relyea, H.A.; Vrtis, J.M.; Woodyer, R.; Rimkus, S.A.; van der Donk, W.A.
Inhibition and pH dependence of phosphite dehydrogenase
Biochemistry
44
6640-6649
2005
Pseudomonas stutzeri
brenda
Relyea, H.A.; van der Donk, W.A.
Mechanism and applications of phosphite dehydrogenase
Bioorg. Chem.
33
171-189
2005
Alcaligenes faecalis, Pseudomonas stutzeri, Pseudomonas stutzeri WM88
brenda
Johannes, T.W.; Woodyer, R.D.; Zhao, H.
Directed evolution of a thermostable phosphite dehydrogenase for NAD(P)H regeneration
Appl. Environ. Microbiol.
71
5728-5734
2005
Pseudomonas stutzeri
brenda
Johannes, T.W.; Woodyer, R.D.; Zhao, H.
Efficient regeneration of NADPH using an engineered phosphite dehydrogenase
Biotechnol. Bioeng.
96
18-26
2007
Pseudomonas stutzeri
brenda
Woodyer, R.; van der Donk, W.A.; Zhao, H.
Optimizing a biocatalyst for improved NAD(P)H regeneration: directed evolution of phosphite dehydrogenase
Comb. Chem. High Throughput Screen.
9
237-245
2006
Pseudomonas stutzeri
brenda
Woodyer, R.; Zhao, H.; van der Donk, W.A.
Mechanistic investigation of a highly active phosphite dehydrogenase mutant and its application for NADPH regeneration
FEBS J.
272
3816-3827
2005
Pseudomonas stutzeri
brenda
Fogle, E.J.; van der Donk, W.A.
Pre-steady-state studies of phosphite dehydrogenase demonstrate that hydride transfer is fully rate limiting
Biochemistry
46
13101-13108
2007
Pseudomonas stutzeri, Pseudomonas stutzeri WW88
brenda
McLachlan, M.J.; Johannes, T.W.; Zhao, H.
Further improvement of phosphite dehydrogenase thermostability by saturation mutagenesis
Biotechnol. Bioeng.
99
268-274
2008
Pseudomonas stutzeri (O69054)
brenda
Liu, D.F.; Ding, H.T.; Du, Y.Q.; Zhao, Y.H.; Jia, X.M.
Cloning, expression, and characterization of a wide-pH-range stable phosphite dehydrogenase from Pseudomonas sp. K in Escherichia coli
Appl. Biochem. Biotechnol.
166
1301-1313
2012
Pseudomonas sp. (F2YGD2), Pseudomonas sp., Pseudomonas sp. K (F2YGD2)
brenda
Hung, J.E.; Fogle, E.J.; Christman, H.D.; Johannes, T.W.; Zhao, H.; Metcalf, W.W.; van der Donk, W.A.
Investigation of the role of Arg301 identified in the X-ray structure of phosphite dehydrogenase
Biochemistry
51
4254-4262
2012
Cupriavidus metallidurans, Cupriavidus metallidurans CH34, Methylorubrum extorquens, Methylorubrum extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1, Nostoc punctiforme, Pseudomonas stutzeri (O69054), Pseudomonas stutzeri
brenda
Zou, Y.; Zhang, H.; Brunzelle, J.S.; Johannes, T.W.; Woodyer, R.; Hung, J.E.; Nair, N.; van der Donk, W.A.; Zhao, H.; Nair, S.K.
Crystal structures of phosphite dehydrogenase provide insights into nicotinamide cofactor regeneration
Biochemistry
51
4263-4270
2012
Pseudomonas stutzeri (O69054)
brenda
Hirota, R.; Yamane, S.T.; Fujibuchi, T.; Motomura, K.; Ishida, T.; Ikeda, T.; Kuroda, A.
Isolation and characterization of a soluble and thermostable phosphite dehydrogenase from Ralstonia sp. strain 4506
J. Biosci. Bioeng.
113
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2012
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